Abstract
By using interactive computer graphics, two models for calmodulin have been constructed based on the structures of two functionally and structurally related proteins, intestinal calcium-binding protein and carp parvalbumin. The two models have been compared and contrasted to the parent proteins with respect to proportion of solvent-exposed hydrophobic residues, solvent-accessible surface area, and side-chain packing. Electrostatic potential surfaces generated for the models suggest a probable binding site for basic amphiphilic alpha-helical peptides located between the last E and F helices in the second domain of calmodulin. Both electrostatic and hydrophobic complementarity can contribute to stabilization of a peptide-protein complex in this region.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 5:44 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 11:49 a.m.) |
Indexed | 1 year, 10 months ago (Oct. 31, 2023, 4:11 p.m.) |
Issued | 40 years, 1 month ago (Aug. 1, 1985) |
Published | 40 years, 1 month ago (Aug. 1, 1985) |
Published Online | 40 years, 1 month ago (Aug. 1, 1985) |
Published Print | 40 years, 1 month ago (Aug. 1, 1985) |
@article{O_Neil_1985, title={A predicted structure of calmodulin suggests an electrostatic basis for its function.}, volume={82}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.82.15.4954}, DOI={10.1073/pnas.82.15.4954}, number={15}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={O’Neil, K T and DeGrado, W F}, year={1985}, month=aug, pages={4954–4958} }